| Overview |
| bs-70532r |
| Integrin _4 (Tyr-1526), Phosphospecific Antibody |
| WB |
| This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose and to unphosphorylated Integrin _4 (Tyr-1526) peptide before affinity purification using phospho-Integrin _4 (Tyr-1526) peptide (without carrier). |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Rabbit |
| Phospho-Integrin _4 (Tyr-1526) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 1526 of human Integrin _4. |
| Tyr-1526 |
| Polyclonal |
| #REF! |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| P16144 |
| integrin, CD104, GP150 |
| The NF-_B/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory I_B proteins. Activation of I_B_ occurs through both serine and tyrosine phosphorylation events. Activation through phosphorylation at Ser-32 and Ser-36 is followed by proteasome-mediated degradation, resulting in the release and nuclear translocation of active NF-_B. This pathway of I_B_ regulation occurs in response to various NF-_B-activating agents, such as TNF_, interleukins, LPS, and irradiation. An alternative pathway for I_B_ regulation occurs through tyrosine phosphorylation of Tyr-42 and Tyr-305. Tyr-42 is phosphorylated in response to oxidative stress and growth factors. This phosphorylation can lead to degradation of I_B_ and NF-_B-activation. In contrast, Tyr-305 phosphorylation by c-Abl has been implicated in I_B_ nuclear translocation and inhibition of NF-_B-activation. Thus, tyrosine phosphorylation of I_B_ may be an important regulatory mechanism in NF-_B signaling. |
| Application Dilution |
| WB |
1:300-5000 |
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